Related Experiment Video

Updated: Jul 1, 2026

Monitoring Functionality and Morphology of Vasculature Recruited by Factors Secreted by Fast-growing Tumor-generating Cells
09:03

Monitoring Functionality and Morphology of Vasculature Recruited by Factors Secreted by Fast-growing Tumor-generating Cells

Published on: November 23, 2014

Functional characterization of filamin a interacting protein 1-like, a novel candidate for antivascular cancer

Mijung Kwon1, Engy Hanna, Dominique Lorang

  • 1Tumor Angiogenesis Section, Surgery Branch, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA.

Cancer Research
|September 17, 2008
PubMed

Insights

Filamin A interacting protein 1-like (FILIP1L) is upregulated by angiogenesis inhibitors. Overexpressing FILIP1L inhibits cancer cell growth and migration, suggesting its potential as an anti-cancer therapeutic.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • Angiogenesis inhibition is a key cancer therapy strategy.
  • Identifying intracellular mediators of this process is crucial.
  • Filamin A interacting protein 1-like (FILIP1L) was identified as upregulated in endothelial cells by angiogenesis inhibitors.

Purpose of the Study:

  • To characterize the expression and subcellular localization of FILIP1L protein.
  • To investigate the function of FILIP1L in cell proliferation, migration, and apoptosis.
  • To evaluate the therapeutic potential of FILIP1L and its mutants in cancer treatment.

Main Methods:

  • Analysis of gene expression profiles in endothelial cells.
  • Characterization of FILIP1L protein expression and localization in human tissues.
  • Overexpression studies of wild-type FILIP1L and its truncation mutants in cells.
  • In vivo studies using targeted expression of FILIP1L mutants in tumor vasculature.

Main Results:

  • FILIP1L protein expression and subcellular localization were described for the first time.
  • FILIP1L overexpression inhibited cell proliferation and migration, and increased apoptosis.
  • A COOH-terminal truncation mutant (FILIP1LΔC103) showed enhanced antiproliferative activity.
  • Targeted expression of FILIP1LΔC103 in tumor vasculature significantly inhibited tumor growth in vivo.

Conclusions:

  • FILIP1L is a novel protein that may mediate the effects of angiogenesis inhibitors.
  • FILIP1L exhibits potent anti-proliferative and anti-migratory functions.
  • FILIP1L, particularly the FILIP1LΔC103 mutant, holds potential as an antivascular reagent for cancer therapy.

More Related Videos

Characterization of Cell Membrane Extensions and Studying Their Roles in Cancer Cell Adhesion Dynamics08:11

Characterization of Cell Membrane Extensions and Studying Their Roles in Cancer Cell Adhesion Dynamics

Published on: March 26, 2018

A 3D Spheroid Model as a More Physiological System for Cancer-Associated Fibroblasts Differentiation and Invasion In Vitro Studies06:27

A 3D Spheroid Model as a More Physiological System for Cancer-Associated Fibroblasts Differentiation and Invasion In Vitro Studies

Published on: August 8, 2019

Related Concept Videos

Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...